MITOS_HUMAN
ID MITOS_HUMAN Reviewed; 735 AA.
AC Q9NUT2; A5D8W3; B2RBL8; B3KND2; B4DG02; G3XAP3; O95787; Q53GM0;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Mitochondrial potassium channel ATP-binding subunit {ECO:0000305};
DE AltName: Full=ATP-binding cassette sub-family B member 8, mitochondrial {ECO:0000303|PubMed:25944712};
DE Short=ABCB8 {ECO:0000303|PubMed:25944712};
DE AltName: Full=Mitochondrial ATP-binding cassette 1 {ECO:0000303|PubMed:9878413};
DE Short=M-ABC1 {ECO:0000303|PubMed:9878413};
DE AltName: Full=Mitochondrial sulfonylurea-receptor {ECO:0000303|PubMed:31435016};
DE Short=MITOSUR {ECO:0000303|PubMed:31435016};
DE Flags: Precursor;
GN Name=ABCB8 {ECO:0000303|PubMed:25944712, ECO:0000312|HGNC:HGNC:49};
GN Synonyms=MABC1 {ECO:0000303|PubMed:9878413},
GN MITOSUR {ECO:0000303|PubMed:31435016};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND MUTAGENESIS.
RX PubMed=9878413; DOI=10.1006/jmbi.1998.2259;
RA Hogue D.L., Liu L., Ling V.;
RT "Identification and characterization of a mammalian mitochondrial ATP-
RT binding cassette membrane protein.";
RL J. Mol. Biol. 285:379-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC TISSUE=Amygdala, Placenta, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TRANSIT PEPTIDE CLEAVAGE SITE.
RX PubMed=16259955; DOI=10.1016/j.bbrc.2005.10.070;
RA Ardehali H., Xue T., Dong P., Machamer C.;
RT "Targeting of the mitochondrial membrane proteins to the cell surface for
RT functional studies.";
RL Biochem. Biophys. Res. Commun. 338:1143-1151(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [9]
RP VARIANT ILE-152.
RX PubMed=11829140; DOI=10.1007/s10038-002-8653-6;
RA Saito S., Iida A., Sekine A., Miura Y., Ogawa C., Kawauchi S., Higuchi S.,
RA Nakamura Y.;
RT "Three hundred twenty-six genetic variations in genes encoding nine members
RT of ATP-binding cassette, subfamily B (ABCB/MDR/TAP), in the Japanese
RT population.";
RL J. Hum. Genet. 47:38-50(2002).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-165 AND GLY-690.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP INDUCTION BY SP1.
RX PubMed=21046154; DOI=10.1007/s00438-010-0586-8;
RA Sachrajda I., Ratajewski M.;
RT "Mithramycin A suppresses expression of the human melanoma-associated gene
RT ABCB8.";
RL Mol. Genet. Genomics 285:57-65(2011).
RN [12]
RP INTERACTION WITH C10ORF88.
RX PubMed=25063848; DOI=10.1096/fj.14-254045;
RA Yang X., Yang J., Li L., Sun L., Yi X., Han X., Si W., Yan R., Chen Z.,
RA Xie G., Li W., Shang Y., Liang J.;
RT "PAAT, a novel ATPase and trans-regulator of mitochondrial ABC
RT transporters, is critically involved in the maintenance of mitochondrial
RT homeostasis.";
RL FASEB J. 28:4821-4834(2014).
RN [13]
RP FUNCTION, AND INTERACTION WITH NRP1.
RX PubMed=30623799; DOI=10.1016/j.isci.2018.12.005;
RA Issitt T., Bosseboeuf E., De Winter N., Dufton N., Gestri G., Senatore V.,
RA Chikh A., Randi A.M., Raimondi C.;
RT "Neuropilin-1 Controls Endothelial Homeostasis by Regulating Mitochondrial
RT Function and Iron-Dependent Oxidative Stress.";
RL IScience 11:205-223(2019).
RN [14]
RP MUTAGENESIS OF LYS-513, FUNCTION, SUBUNIT, TOPOLOGY, ACTIVITY REGULATION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=31435016; DOI=10.1038/s41586-019-1498-3;
RA Paggio A., Checchetto V., Campo A., Menabo R., Di Marco G., Di Lisa F.,
RA Szabo I., Rizzuto R., De Stefani D.;
RT "Identification of an ATP-sensitive potassium channel in mitochondria.";
RL Nature 572:609-613(2019).
RN [15] {ECO:0007744|PDB:5OCH}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 110-714 IN COMPLEX WITH ADP.
RA Faust B., Pike A.C.W., Shintre C.A., Quiqley A.M., Chu A., Barr A.,
RA Shrestha L., Mukhopadhyay S., Borkowska O., Chalk R., Burgess-Brown N.A.,
RA Arrowsmith C.H., Edwards A.M., Bountra C., Carpenter E.P.;
RT "The crystal structure of human ABCB8 in an outward-facing state.";
RL Submitted (JUN-2017) to the PDB data bank.
CC -!- FUNCTION: ATP-binding subunit of the mitochondrial potassium channel
CC located in the mitochondrial inner membrane (PubMed:31435016). Together
CC with CCDC51/MITOK, forms a protein complex localized in the
CC mitochondria that mediates ATP-dependent potassium currents across the
CC inner membrane (that is, mitoK(ATP) channel) (PubMed:31435016). Plays a
CC role in mitochondrial iron transport (PubMed:30623799). Required for
CC maintenance of normal cardiac function, possibly by influencing
CC mitochondrial iron export and regulating the maturation of cytosolic
CC iron sulfur cluster-containing enzymes (By similarity).
CC {ECO:0000250|UniProtKB:Q9CXJ4, ECO:0000269|PubMed:30623799,
CC ECO:0000269|PubMed:31435016}.
CC -!- ACTIVITY REGULATION: Channel activity inhibited by ATP via
CC ABCB8/MITOSUR subunit. {ECO:0000269|PubMed:31435016}.
CC -!- SUBUNIT: The mitochondrial potassium channel (mitoK(ATP)) is composed
CC of 4 subunits of CCDC51/MITOK and 4 subunits of ABCB8/MITOSUR
CC (Probable). Interacts with C10orf88/PAAT (PubMed:25063848). Interacts
CC with NRP1; NRP1 regulates ABCB8/MITOSUR protein levels in mitochondria
CC (PubMed:30623799). {ECO:0000269|PubMed:25063848,
CC ECO:0000269|PubMed:30623799, ECO:0000305|PubMed:31435016}.
CC -!- INTERACTION:
CC Q9NUT2; Q96ER9: CCDC51; NbExp=2; IntAct=EBI-722515, EBI-11926384;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:16259955, ECO:0000269|PubMed:31435016}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Long;
CC IsoId=Q9NUT2-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9NUT2-2; Sequence=VSP_000026;
CC Name=3;
CC IsoId=Q9NUT2-3; Sequence=VSP_000026, VSP_055297;
CC Name=4;
CC IsoId=Q9NUT2-4; Sequence=VSP_056745;
CC Name=5;
CC IsoId=Q9NUT2-5; Sequence=VSP_056744;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- INDUCTION: SP1 transcription factor binds to the ABCB8 core promoter
CC region, possibly regulating its transcription.
CC {ECO:0000269|PubMed:21046154, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=ABCMdb; Note=Database for mutations in ABC proteins;
CC URL="http://abcm2.hegelab.org/search";
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DR EMBL; AF047690; AAD15748.1; -; mRNA.
DR EMBL; AK002018; BAA92038.1; -; mRNA.
DR EMBL; AK024401; BAG51294.1; -; mRNA.
DR EMBL; AK222911; BAD96631.1; -; mRNA.
DR EMBL; AK294344; BAG57613.1; -; mRNA.
DR EMBL; AK314721; BAG37265.1; -; mRNA.
DR EMBL; AC010973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471173; EAW54057.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54061.1; -; Genomic_DNA.
DR EMBL; CH471173; EAW54062.1; -; Genomic_DNA.
DR EMBL; BC141814; AAI41815.1; -; mRNA.
DR EMBL; BC141836; AAI41837.1; -; mRNA.
DR EMBL; BC151235; AAI51236.1; -; mRNA.
DR CCDS; CCDS5913.1; -. [Q9NUT2-2]
DR CCDS; CCDS64798.1; -. [Q9NUT2-4]
DR CCDS; CCDS64799.1; -. [Q9NUT2-1]
DR CCDS; CCDS64800.1; -. [Q9NUT2-3]
DR RefSeq; NP_001269220.1; NM_001282291.1. [Q9NUT2-1]
DR RefSeq; NP_001269221.1; NM_001282292.1. [Q9NUT2-3]
DR RefSeq; NP_001269222.1; NM_001282293.1. [Q9NUT2-4]
DR RefSeq; NP_009119.2; NM_007188.4. [Q9NUT2-2]
DR PDB; 5OCH; X-ray; 3.40 A; A/B/C/D/E/F/G/H=110-714.
DR PDB; 7EHL; EM; -; A/B=58-735.
DR PDBsum; 5OCH; -.
DR PDBsum; 7EHL; -.
DR AlphaFoldDB; Q9NUT2; -.
DR SMR; Q9NUT2; -.
DR BioGRID; 116364; 65.
DR ComplexPortal; CPX-6083; MITOK-MITOSUR mitochondrial potassium channel complex.
DR IntAct; Q9NUT2; 22.
DR MINT; Q9NUT2; -.
DR STRING; 9606.ENSP00000297504; -.
DR DrugBank; DB00997; Doxorubicin.
DR TCDB; 3.A.1.201.22; the atp-binding cassette (abc) superfamily.
DR iPTMnet; Q9NUT2; -.
DR PhosphoSitePlus; Q9NUT2; -.
DR BioMuta; ABCB8; -.
DR DMDM; 143811358; -.
DR EPD; Q9NUT2; -.
DR jPOST; Q9NUT2; -.
DR MassIVE; Q9NUT2; -.
DR MaxQB; Q9NUT2; -.
DR PaxDb; Q9NUT2; -.
DR PeptideAtlas; Q9NUT2; -.
DR PRIDE; Q9NUT2; -.
DR ProteomicsDB; 33804; -.
DR ProteomicsDB; 719; -.
DR ProteomicsDB; 82718; -. [Q9NUT2-1]
DR ProteomicsDB; 82719; -. [Q9NUT2-2]
DR Antibodypedia; 32942; 194 antibodies from 28 providers.
DR DNASU; 11194; -.
DR Ensembl; ENST00000297504.10; ENSP00000297504.6; ENSG00000197150.13. [Q9NUT2-1]
DR Ensembl; ENST00000358849.9; ENSP00000351717.4; ENSG00000197150.13. [Q9NUT2-2]
DR Ensembl; ENST00000498578.5; ENSP00000418271.1; ENSG00000197150.13. [Q9NUT2-3]
DR Ensembl; ENST00000542328.5; ENSP00000438776.1; ENSG00000197150.13. [Q9NUT2-4]
DR GeneID; 11194; -.
DR KEGG; hsa:11194; -.
DR MANE-Select; ENST00000358849.9; ENSP00000351717.4; NM_007188.5; NP_009119.2. [Q9NUT2-2]
DR UCSC; uc003wik.6; human. [Q9NUT2-1]
DR CTD; 11194; -.
DR DisGeNET; 11194; -.
DR GeneCards; ABCB8; -.
DR HGNC; HGNC:49; ABCB8.
DR HPA; ENSG00000197150; Low tissue specificity.
DR MIM; 605464; gene.
DR neXtProt; NX_Q9NUT2; -.
DR OpenTargets; ENSG00000197150; -.
DR PharmGKB; PA24390; -.
DR VEuPathDB; HostDB:ENSG00000197150; -.
DR eggNOG; KOG0058; Eukaryota.
DR GeneTree; ENSGT00940000159126; -.
DR HOGENOM; CLU_000604_84_3_1; -.
DR InParanoid; Q9NUT2; -.
DR OMA; FNTLQMG; -.
DR OrthoDB; 684058at2759; -.
DR PhylomeDB; Q9NUT2; -.
DR TreeFam; TF105196; -.
DR BRENDA; 7.4.2.5; 2681.
DR PathwayCommons; Q9NUT2; -.
DR Reactome; R-HSA-1369007; Mitochondrial ABC transporters.
DR SignaLink; Q9NUT2; -.
DR BioGRID-ORCS; 11194; 13 hits in 1082 CRISPR screens.
DR ChiTaRS; ABCB8; human.
DR GeneWiki; ABCB8; -.
DR GenomeRNAi; 11194; -.
DR Pharos; Q9NUT2; Tbio.
DR PRO; PR:Q9NUT2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9NUT2; protein.
DR Bgee; ENSG00000197150; Expressed in pancreatic ductal cell and 125 other tissues.
DR ExpressionAtlas; Q9NUT2; baseline and differential.
DR Genevisible; Q9NUT2; HS.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; TAS:ProtInc.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0062157; C:mitochondrial ATP-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006884; P:cell volume homeostasis; IDA:ComplexPortal.
DR GO; GO:0140141; P:mitochondrial potassium ion transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Ion transport; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Potassium;
KW Potassium transport; Reference proteome; Transit peptide; Transmembrane;
KW Transmembrane helix; Transport.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 26..735
FT /note="Mitochondrial potassium channel ATP-binding subunit"
FT /evidence="ECO:0000255"
FT /id="PRO_0000000251"
FT TOPO_DOM 26..144
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:31435016"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 166..195
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:31435016"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 217..295
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305|PubMed:31435016"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00441"
FT TOPO_DOM 317..735
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:31435016"
FT DOMAIN 150..437
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 472..709
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 712..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 507..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434,
FT ECO:0000269|Ref.15, ECO:0007744|PDB:5OCH"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056744"
FT VAR_SEQ 1..153
FT /note="MLVHLFRVGIRGGPFPGRLLPPLRFQTFSAVRNTWRNGKTGQLHKAEGEYSD
FT GYRSSSLLRAVAHLRSQLWAHLPRAPLAPRWSPSAWCWVGGALLGPMVLSKHPHLCLVA
FT LCEAEEAPPASSTPHVVGSRFNWKLFWQFLHPHLLVLGVAVV -> MRVKLLLPAAPVL
FT PRQHAGAFISGRDSGWPIPRQAATAPPLPDILSCQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056745"
FT VAR_SEQ 33..49
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9878413,
FT ECO:0000303|Ref.3"
FT /id="VSP_000026"
FT VAR_SEQ 665..689
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055297"
FT VARIANT 152
FT /note="V -> I (in dbSNP:rs4148844)"
FT /evidence="ECO:0000269|PubMed:11829140"
FT /id="VAR_013331"
FT VARIANT 165
FT /note="I -> T (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035733"
FT VARIANT 690
FT /note="A -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035734"
FT MUTAGEN 512..513
FT /note="GK->AR: Renders the protein unstable."
FT /evidence="ECO:0000269|PubMed:9878413"
FT MUTAGEN 513
FT /note="K->A: Abolish binding to ATP."
FT /evidence="ECO:0000269|PubMed:31435016"
FT CONFLICT 174
FT /note="E -> K (in Ref. 1; AAD15748)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="D -> N (in Ref. 1; AAD15748)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="T -> S (in Ref. 1; AAD15748)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="M -> T (in Ref. 2; BAG57613)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="Q -> H (in Ref. 1; AAD15748)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="F -> L (in Ref. 1; AAD15748)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="R -> H (in Ref. 2; BAA92038)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="F -> Y (in Ref. 2; BAG57613)"
FT /evidence="ECO:0000305"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:5OCH"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 145..171
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 190..237
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 248..279
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 291..309
FT /evidence="ECO:0007829|PDB:5OCH"
FT TURN 311..313
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 316..339
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 350..395
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:5OCH"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 408..430
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 432..449
FT /evidence="ECO:0007829|PDB:5OCH"
FT TURN 465..467
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 472..480
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 482..497
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 513..520
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 527..533
FT /evidence="ECO:0007829|PDB:5OCH"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 543..549
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 565..569
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 578..587
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 591..594
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 597..599
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 600..602
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 604..610
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 614..626
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 631..637
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 644..657
FT /evidence="ECO:0007829|PDB:5OCH"
FT TURN 658..660
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 661..666
FT /evidence="ECO:0007829|PDB:5OCH"
FT TURN 670..672
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 673..675
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 676..683
FT /evidence="ECO:0007829|PDB:5OCH"
FT STRAND 686..691
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 693..698
FT /evidence="ECO:0007829|PDB:5OCH"
FT HELIX 702..714
FT /evidence="ECO:0007829|PDB:5OCH"
SQ SEQUENCE 735 AA; 79989 MW; B7E02B063E6C6F3B CRC64;
MLVHLFRVGI RGGPFPGRLL PPLRFQTFSA VRNTWRNGKT GQLHKAEGEY SDGYRSSSLL
RAVAHLRSQL WAHLPRAPLA PRWSPSAWCW VGGALLGPMV LSKHPHLCLV ALCEAEEAPP
ASSTPHVVGS RFNWKLFWQF LHPHLLVLGV AVVLALGAAL VNVQIPLLLG QLVEVVAKYT
RDHVGSFMTE SQNLSTHLLI LYGVQGLLTF GYLVLLSHVG ERMAVDMRRA LFSSLLRQDI
TFFDANKTGQ LVSRLTTDVQ EFKSSFKLVI SQGLRSCTQV AGCLVSLSML STRLTLLLMV
ATPALMGVGT LMGSGLRKLS RQCQEQIARA MGVADEALGN VRTVRAFAME QREEERYGAE
LEACRCRAEE LGRGIALFQG LSNIAFNCMV LGTLFIGGSL VAGQQLTGGD LMSFLVASQT
VQRSMANLSV LFGQVVRGLS AGARVFEYMA LNPCIPLSGG CCVPKEQLRG SVTFQNVCFS
YPCRPGFEVL KDFTLTLPPG KIVALVGQSG GGKTTVASLL ERFYDPTAGV VMLDGRDLRT
LDPSWLRGQV VGFISQEPVL FGTTIMENIR FGKLEASDEE VYTAAREANA HEFITSFPEG
YNTVVGERGT TLSGGQKQRL AIARALIKQP TVLILDEATS ALDAESERVV QEALDRASAG
RTVLVIAHRL STVRGAHCIV VMADGRVWEA GTHEELLKKG GLYAELIRRQ ALDAPRTAAP
PPKKPEGPRS HQHKS
